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Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution

Author

Listed:
  • Nadav Elad

    (Weizmann Institute of Science)

  • Szilvia Baron

    (Weizmann Institute of Science)

  • Yoav Peleg

    (Weizmann Institute of Science)

  • Shira Albeck

    (Weizmann Institute of Science)

  • Jacob Grunwald

    (Weizmann Institute of Science)

  • Gal Raviv

    (Weizmann Institute of Science)

  • Zippora Shakked

    (Weizmann Institute of Science)

  • Oren Zimhony

    (Hebrew University)

  • Ron Diskin

    (Weizmann Institute of Science)

Abstract

Tuberculosis (TB) is a devastating and rapidly spreading disease caused by Mycobacterium tuberculosis (Mtb). Therapy requires prolonged treatment with a combination of multiple agents and interruptions in the treatment regimen result in emergence and spread of multi-drug resistant (MDR) Mtb strains. MDR Mtb poses a significant global health problem, calling for urgent development of novel drugs to combat TB. Here, we report the 3.3 Å resolution structure of the ~2 MDa type-I fatty acid synthase (FAS-I) from Mtb, determined by single particle cryo-EM. Mtb FAS-I is an essential enzymatic complex that contributes to the virulence of Mtb, and thus a prime target for anti-TB drugs. The structural information for Mtb FAS-I we have obtained enables computer-based drug discovery approaches, and the resolution achieved by cryo-EM is sufficient for elucidating inhibition mechanisms by putative small molecular weight inhibitors.

Suggested Citation

  • Nadav Elad & Szilvia Baron & Yoav Peleg & Shira Albeck & Jacob Grunwald & Gal Raviv & Zippora Shakked & Oren Zimhony & Ron Diskin, 2018. "Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution," Nature Communications, Nature, vol. 9(1), pages 1-6, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06440-6
    DOI: 10.1038/s41467-018-06440-6
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